ID   CYAA_PROMI              Reviewed;         865 AA.
AC   Q59685;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Adenylate cyclase;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase;
DE   AltName: Full=Adenylyl cyclase;
GN   Name=cya;
OS   Proteus mirabilis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8874804; DOI=10.1016/0300-9084(96)82192-4;
RA   Trotot P., Sismeiro O., Vivares C., Glaser P., Bresson-Roy A., Danchin A.;
RT   "Comparative analysis of the cya locus in enterobacteria and related Gram-
RT   negative facultative anaerobes.";
RL   Biochimie 78:277-287(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; U22969; AAC44330.1; -; Genomic_DNA.
DR   RefSeq; WP_004246330.1; NZ_WEKK01000020.1.
DR   AlphaFoldDB; Q59685; -.
DR   STRING; 584.AOUC001_17900; -.
DR   GeneID; 6803142; -.
DR   PATRIC; fig|584.120.peg.92; -.
DR   OMA; YDDYVMS; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000274; Adenylate_cyclase_1.
DR   InterPro; IPR024686; Adenylate_cyclase_1_CS.
DR   InterPro; IPR024685; Adenylate_cyclase_1_N.
DR   PANTHER; PTHR38760; PTHR38760; 1.
DR   Pfam; PF12633; Adenyl_cycl_N; 1.
DR   Pfam; PF01295; Adenylate_cycl; 1.
DR   PIRSF; PIRSF001444; Adenylate_cycl; 1.
DR   PROSITE; PS01092; ADENYLATE_CYCLASE_1_1; 1.
DR   PROSITE; PS01093; ADENYLATE_CYCLASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; cAMP biosynthesis; Cytoplasm; Lyase; Nucleotide-binding.
FT   CHAIN           1..865
FT                   /note="Adenylate cyclase"
FT                   /id="PRO_0000195678"
FT   REGION          1..540
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255"
FT   REGION          546..865
FT                   /note="Regulatory"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   865 AA;  99450 MW;  99D4B1DD51FCB7D7 CRC64;
     MYLYIETLKQ RLDAINQLRL ERAFASMSDV FKQVYGLIPV LLHYHHPQLP GYIQGNVPHG
     TCFFEPDDVQ RQWVNKLTNA SCDEPMNGYT SGELPITGIY SMGSTSSIGQ SHCSDIDIWV
     CHQSWLDQDE RARLQRKCLL IEQWAGELGI DVTFFLIDEN RFRHHASGSL GGEDCGSTQH
     ILLLDEFYRT AVRLAGKRLL WTMVPVEEEY HYDEYVNSLY AQGVLTPNEW LDLGGLGELS
     AEEYFGASLW QLYKSVDSPY KAVLKSILLE AYSADYPNGK LLALEMKQHL HRGEIVNYGL
     DAYCMMLERV TRYLVSINDL TRLDLIRRCF YLKVCEKLSN EKNENEPAGW RRQVLSQLVT
     QWQWDHERLA ILDNRDSWKI ERVRNAHNEL LDTMMQSYRN LIRFARRNNL SVSASPQDIG
     VLTRKLYAAF EALPGKVTLV NPQISPDLSE PHLTFIYVPP GRANRSGWYL YNRAPDFAHI
     VGHQPLEYNR YLNKLVAWSY FNGLLTKDSQ VYIHQGDSSC DEIKLHELVR DISSHFPIRL
     PAPTPKALYS PCEIRHLAII VNLEVDPTER FSDQVVHFDF RKLDVFSFGE EEQCLIGSID
     LLYRNSWNEV RTLHFNGTQS MLESLKTILG KMHQDAAPPA SVEVFCYSQH LRGLIRTRVQ
     QLVSECIELR LSTNRLEPGR FKALRIAGQT WGLFFERLNV SVQKLENAIE FYGAISYNKL
     HGLPVKLGKD ARYLPAVIDG FACEGIIQFF FETTEDNNVF NIYILDEANR VEIYSHCEGS
     KEELVKDVSR FYSSSHDRFT YGSSFINFNL PQFYQIVKVD GATQVLPFAG GSFGKLSDLG
     KTAPKEEMST KPIQGFNDYQ AVHHH